A recombinant carboxy-terminal domain of the protective antigen of Bacillus anthracis protects mice against anthrax infection.
about
Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactionsBinary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteinsHuman monoclonal antibodies against anthrax lethal factor and protective antigen act independently to protect against Bacillus anthracis infection and enhance endogenous immunity to anthraxAnthrax prophylaxis: recent advances and future directionsAnalysis of antibody responses to protective antigen-based anthrax vaccines through use of competitive assaysPrinciples of antidote pharmacology: an update on prophylaxis, post-exposure treatment recommendations and research initiatives for biological agentsRabies virus glycoprotein as a carrier for anthrax protective antigenInduction of neutralizing antibody responses to anthrax protective antigen by using influenza virus vectors: implications for disparate immune system priming pathwaysImmunogenicity of recombinant protective antigen and efficacy against aerosol challenge with anthrax.Distribution of productive antigen-processing activity for MHC class II presentation in macrophages.Recombinant protective antigen 102 (rPA102): profile of a second-generation anthrax vaccine.Complement C3d conjugation to anthrax protective antigen promotes a rapid, sustained, and protective antibody response.Immunogenicity of Bacillus anthracis protective antigen domains and efficacy of elicited antibody responses depend on host genetic background.A single immunization with a dry powder anthrax vaccine protects rabbits against lethal aerosol challengeNew classes of orthopoxvirus vaccine candidates by functionally screening a synthetic library for protective antigens.Chimeric influenza virus hemagglutinin proteins containing large domains of the Bacillus anthracis protective antigen: protein characterization, incorporation into infectious influenza viruses, and antigenicity.Select human anthrax protective antigen epitope-specific antibodies provide protection from lethal toxin challenge.Cytokine response and survival of mice immunized with an adenovirus expressing Bacillus anthracis protective antigen domain 4.An anthrax subunit vaccine candidate based on protective regions of Bacillus anthracis protective antigen and lethal factor.A single-dose PLGA encapsulated protective antigen domain 4 nanoformulation protects mice against Bacillus anthracis spore challenge.Venezuelan equine encephalitis virus-vectored vaccines protect mice against anthrax spore challenge.A monoclonal antibody to Bacillus anthracis protective antigen defines a neutralizing epitope in domain 1Development of an improved vaccine for anthraxVaccines for Category A bioterrorism diseases.Salmonella enterica serovar typhimurium expressing a chromosomally integrated copy of the Bacillus anthracis protective antigen gene protects mice against an anthrax spore challenge.Oral administration of a Salmonella enterica-based vaccine expressing Bacillus anthracis protective antigen confers protection against aerosolized B. anthracis.Enhanced Immune Response to DNA Vaccine Encoding Bacillus anthracis PA-D4 Protects Mice against Anthrax Spore Challenge.Analysis of epitope information related to Bacillus anthracis and Clostridium botulinum.Human monoclonal antibodies generated following vaccination with AVA provide neutralization by blocking furin cleavage but not by preventing oligomerizationProtection against anthrax toxemia by hexa-D-arginine in vitro and in vivo.Detoxified lethal toxin as a potential mucosal vaccine against anthrax.Potential biological targets of Bacillus anthracis in anti-infective approaches against the threat of bioterrorism.Frequency and domain specificity of toxin-neutralizing paratopes in the human antibody response to anthrax vaccine adsorbedIdentification of linear epitopes in Bacillus anthracis protective antigen bound by neutralizing antibodies.Anthrax, toxins and vaccines: a 125-year journey targeting Bacillus anthracis.Recombinant Sindbis virus vectors designed to express protective antigen of Bacillus anthracis protect animals from anthrax and display synergy with ciprofloxacin.Adaptation of the endogenous Salmonella enterica serovar Typhi clyA-encoded hemolysin for antigen export enhances the immunogenicity of anthrax protective antigen domain 4 expressed by the attenuated live-vector vaccine strain CVD 908-htrA.Anthrax vaccines: present status and future prospects.Human monoclonal antibody AVP-21D9 to protective antigen reduces dissemination of the Bacillus anthracis Ames strain from the lungs in a rabbit modelDifferential processing of CD4 T-cell epitopes from the protective antigen of Bacillus anthracis.
P2860
Q24295221-283A844B-AE42-435A-BF35-6E444831FD52Q24562788-6687E005-3C82-4104-ABA8-2667132FE023Q24682011-666B833A-A262-4D61-B959-05FF474F41AEQ26781366-8BB421BB-ABD2-4164-A90F-96116C776E00Q28383562-0B889B45-61EF-4167-9C1F-578AE39FD5C8Q28384852-5BB01338-615E-4105-BEE9-F17E3BEB99C6Q28391261-7B2CE433-E392-4BB9-BC00-9E1AE5B85029Q28397551-FBDEB6FA-C4C2-46C4-85AC-DDC7DEC56608Q30859738-D38EE0CF-4B9A-42ED-A213-7A90D422813DQ33223830-ACBCCBF5-CB40-44E0-9C0A-AD01470AAFCCQ33258307-C0C4CAD1-1CD2-4DAC-8921-FD1B5695362EQ33302902-6838DC38-9575-49AB-8C55-CAFA03D90102Q33334776-0869F142-8FB6-42D8-ABE9-D0D281836A20Q33360151-B38E1A25-D8C9-40BA-B277-A75DCD0834CEQ33508318-05115201-C79B-4B6C-8E81-9FE9E24049CAQ33908690-DC542943-9BF0-44B9-A6E5-D0491F02CF1BQ33936452-48A33543-70DF-48E3-B683-A88B96158B50Q34334441-9F39E3E5-3983-4298-A5A1-04211EF006D7Q34433313-8AF3C07B-848A-43D5-9DF2-984789C8691DQ34700706-E41E07F2-5892-494B-B757-1EBDE243E64DQ34714912-3668F225-4A13-4807-98E2-9CA380DD06B6Q34721109-D1B5EF8C-B898-4E1C-82BD-38F231CBF2CDQ34744925-29222C0C-1D19-4948-B320-695F1BA6DE8FQ35040844-BC47EC77-AC80-4BA5-8F1F-A94CD2A8A413Q35106528-2DCF38EA-9392-418B-9D33-5A8F7F857D56Q35783791-AAB87E3E-9026-4C06-B30A-4FF4581CCFDFQ35796747-5700389A-BA98-41AF-ACFD-EC2523503368Q35869311-22133BFC-CCB1-4D05-A154-48DA3F84AEDEQ36007463-D20A45D5-AA6E-43DA-AF1F-8DFFA7C4D91DQ36228556-85122E22-CBF4-4CE3-821F-87C648F756B6Q36539063-E1F3E8A2-8CA7-46B1-8D39-B8F98B227770Q36901955-DB8360DA-CC86-4B81-BA30-39D9FA1C8375Q37191250-CA004FA6-D383-4D12-947D-5C62EE5B9E1EQ37375729-8D636CA6-5912-4C26-B2CD-DF1773813517Q37404847-205F891D-E544-4089-A8B9-BB29D758ECEFQ37410033-030AFA61-FC70-4E26-AE80-C8315E220B26Q37623663-86CD2149-7B66-4D9E-B6E2-E7870F7E3549Q38132268-190D518A-5AB8-49B8-AEFA-1A693BFBC91AQ41869569-8E7027F7-882F-41C9-B289-50EEFE2063A6Q44619427-301B2E24-1EBD-4E07-8FCC-220745EC5827
P2860
A recombinant carboxy-terminal domain of the protective antigen of Bacillus anthracis protects mice against anthrax infection.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
A recombinant carboxy-terminal ...... ice against anthrax infection.
@ast
A recombinant carboxy-terminal ...... ice against anthrax infection.
@en
A recombinant carboxy-terminal ...... ice against anthrax infection.
@nl
type
label
A recombinant carboxy-terminal ...... ice against anthrax infection.
@ast
A recombinant carboxy-terminal ...... ice against anthrax infection.
@en
A recombinant carboxy-terminal ...... ice against anthrax infection.
@nl
prefLabel
A recombinant carboxy-terminal ...... ice against anthrax infection.
@ast
A recombinant carboxy-terminal ...... ice against anthrax infection.
@en
A recombinant carboxy-terminal ...... ice against anthrax infection.
@nl
P2093
P2860
P1476
A recombinant carboxy-terminal ...... ice against anthrax infection.
@en
P2093
E Diane Williamson
Helen Bullifent
Helen C Flick-Smith
Julie Miller
Nicola J Walker
Paula Gibson
Sarah Hayward
P2860
P304
P356
10.1128/IAI.70.3.1653-1656.2002
P407
P577
2002-03-01T00:00:00Z